GMP reductase 1 (GMPR)
The protein contains 345 amino acids for an estimated molecular weight of 37419 Da.
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. (updated: Feb. 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs760571328 | |
| dbSNP:rs1042391 |
The reference OMIM entry for this protein is 139265
Guanosine monophosphate reductase; gmpr
Guanosine monophosphate reductase 1; gmpr1
Gmp reductase
DESCRIPTION
Guanosine monophosphate reductase (EC 1.7.1.7) catalyzes the irreversible NADPH-dependent reductive deamination of guanosine monophosphate (GMP) to inosine monophosphate (IMP). GMPR is able to convert guanosine nucleotides to the pivotal precursor of both guanine (G) and adenine (A) nucleotides. It plays an important role in maintaining the intracellular balance of A and G nucleotides.CLONING
Beutler et al. (1990) and Mason et al. (1990) presented evidence that a gene mapped to chromosome 6 by Kanno et al. (1989) was GMP reductase. Henikoff and Smith (1989) had pointed out similarities between the sequence described by Kanno et al. (1989) for the chromosome 6-encoded gene and the sequence of E. coli GMP reductase. Kondoh et al. (1991) found that the GMPR gene encodes a deduced 345-amino acid protein. By Northern blot analysis, Deng et al. (2002) detected relatively high levels of both GMPR1 and GMPR2 (610781) in heart, skeletal muscle, and kidney, and relatively low levels of both in colon, thymus, and peripheral blood leukocyte. Strong signals of GMPR2 were detected in brain, liver, and placenta, whereas weak signals of GMPR1 were observed in these tissues.GENE STRUCTURE
Kondoh et al. (1991) determined that the GMPR gene spans about 50 kb and contains 9 exons. The gene contains 2 potential Sp1 binding sites within exon 1, and a functional, atypical polyadenylation signal in exon 9.MAPPING
By fluorescence in situ hybridization, Murano et al. (1994) mapped the GMPR gene to 6p23.HISTORY
Kanno et al. (1989) suggested that red cell G6PD (305900) is a fusion protein consisting of an NH2-terminus encoded by chromosome 6 and a COOH-portion coded by an X chromosome. This was subsequently disproved by Beutler et al. (1990) and by Mason et al. (1990). ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 139265 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed